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Protein

Sarcoplasmic/endoplasmic reticulum calcium ATPase 2

Gene

ATP2A2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Isoform 2 is involved in the regulation of the contraction/relaxation cycle (PubMed:16402920). Acts as a regulator of TNFSF11-mediated Ca2+ signaling pathways via its interaction with TMEM64 which is critical for the TNFSF11-induced CREB1 activation and mitochondrial ROS generation necessary for proper osteoclast generation. Association between TMEM64 and SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation of NFATC1 and production of mitochondrial ROS, thereby triggering Ca (2+) signaling cascades that promote osteoclast differentiation and activation (By similarity).By similarity1 Publication

Catalytic activityi

ATP + H2O + Ca2+(Side 1) = ADP + phosphate + Ca2+(Side 2).

Enzyme regulationi

Reversibly inhibited by phospholamban (PLN) at low calcium concentrations (By similarity). Inhibited by sarcolipin (SLN) and myoregulin (MRLN) (By similarity). Enhanced by DWORF; DWORF increases activity by displacing sarcolipin (SLN), phospholamban (PLN) and myoregulin (MRLN) (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi304Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi305Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi307Calcium 2; via carbonyl oxygenBy similarity1
Metal bindingi309Calcium 2By similarity1
Active sitei3514-aspartylphosphate intermediateBy similarity1
Metal bindingi702MagnesiumBy similarity1
Metal bindingi706MagnesiumBy similarity1
Metal bindingi767Calcium 1By similarity1
Metal bindingi770Calcium 1By similarity1
Metal bindingi795Calcium 2By similarity1
Metal bindingi798Calcium 1By similarity1
Metal bindingi799Calcium 1By similarity1
Metal bindingi799Calcium 2By similarity1
Metal bindingi907Calcium 1By similarity1

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • calcium ion binding Source: BHF-UCL
  • calcium-transporting ATPase activity Source: BHF-UCL
  • calcium-transporting ATPase activity involved in regulation of cardiac muscle cell membrane potential Source: BHF-UCL
  • enzyme binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Calcium transport, Ion transport, Transport

Keywords - Ligandi

ATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS10797-MONOMER.
ReactomeiR-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-418359. Reduction of cytosolic Ca++ levels.
R-HSA-5578775. Ion homeostasis.
R-HSA-936837. Ion transport by P-type ATPases.
SignaLinkiP16615.
SIGNORiP16615.

Protein family/group databases

TCDBi3.A.3.2.7. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (EC:3.6.3.8)
Short name:
SERCA2
Short name:
SR Ca(2+)-ATPase 2
Alternative name(s):
Calcium pump 2
Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform
Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Gene namesi
Name:ATP2A2
Synonyms:ATP2B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:812. ATP2A2.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 48CytoplasmicBy similarityAdd BLAST48
Transmembranei49 – 69Helical; Name=1By similarityAdd BLAST21
Topological domaini70 – 89LumenalBy similarityAdd BLAST20
Transmembranei90 – 110Helical; Name=2By similarityAdd BLAST21
Topological domaini111 – 253CytoplasmicBy similarityAdd BLAST143
Transmembranei254 – 273Helical; Name=3By similarityAdd BLAST20
Topological domaini274 – 295LumenalBy similarityAdd BLAST22
Transmembranei296 – 313Helical; Name=4By similarityAdd BLAST18
Topological domaini314 – 756CytoplasmicBy similarityAdd BLAST443
Transmembranei757 – 776Helical; Name=5By similarityAdd BLAST20
Topological domaini777 – 786LumenalBy similarity10
Transmembranei787 – 807Helical; Name=6By similarityAdd BLAST21
Topological domaini808 – 827CytoplasmicBy similarityAdd BLAST20
Transmembranei828 – 850Helical; Name=7By similarityAdd BLAST23
Topological domaini851 – 896LumenalBy similarityAdd BLAST46
Transmembranei897 – 916Helical; Name=8By similarityAdd BLAST20
Topological domaini917 – 929CytoplasmicBy similarityAdd BLAST13
Transmembranei930 – 948Helical; Name=9By similarityAdd BLAST19
Topological domaini949 – 963LumenalBy similarityAdd BLAST15
Transmembranei964 – 984Helical; Name=10By similarityAdd BLAST21
Topological domaini985 – 1042CytoplasmicBy similarityAdd BLAST58

GO - Cellular componenti

  • calcium ion-transporting ATPase complex Source: BHF-UCL
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: Ensembl
  • integral component of plasma membrane Source: ProtInc
  • longitudinal sarcoplasmic reticulum Source: BHF-UCL
  • membrane Source: MGI
  • perinuclear region of cytoplasm Source: Ensembl
  • platelet dense tubular network membrane Source: Reactome
  • protein complex Source: Ensembl
  • ribbon synapse Source: Ensembl
  • sarcoplasmic reticulum Source: BHF-UCL
  • sarcoplasmic reticulum membrane Source: BHF-UCL
  • vesicle membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane, Sarcoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Acrokeratosis verruciformis (AKV)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA localized disorder of keratinization, which is inherited as an autosomal dominant trait. Its onset is early in life with multiple flat-topped, flesh-colored papules on the hands and feet, punctate keratoses on the palms and soles, with varying degrees of nail involvement. The histopathology shows a distinctive pattern of epidermal features with hyperkeratosis, hypergranulosis and acanthosis together with papillomatosis. These changes are frequently associated with circumscribed elevations of the epidermis that are said to resemble church spires. There are no features of dyskeratosis or acantholysis, the typical findings in lesions of Darier disease.
See also OMIM:101900
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017532602P → L in AKV; loss of activity. 1 PublicationCorresponds to variant rs121912737dbSNPEnsembl.1
Darier disease (DD)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA skin disorder characterized by warty papules and plaques in seborrheic areas (central trunk, flexures, scalp and forehead), palmoplantar pits and distinctive nail abnormalities. It is due to loss of adhesion between epidermal cells (acantholysis) and abnormal keratinization. Patients with mild disease may have no more than a few scattered keratotic papules or subtle nail changes, whereas those with severe disease are handicapped by widespread malodorous keratotic plaques. Some patients present with hemorrhage into acantholytic vesicles on the palms and dorsal aspects of the fingers which gives rise to black macules. In a few families affected by Darier disease, neuropsychiatric abnormalities such as mild mental retardation, schizophrenia, bipolar disorder and epilepsy have been reported. Stress, UV exposure, heat, sweat, friction and oral contraception exacerbate disease symptoms. Clinical variants of Darier disease include hypertrophic, vesicobullous, hypopigmented, cornifying, zosteriform or linear, acute and comedonal subtypes. Comedonal Darier disease is characterized by the coexistence of acne-like comedonal lesions with typical Darier hyperkeratotic papules on light-exposed areas. At histopathologic level, comedonal Darier disease differs from classic Darier disease in the prominent follicular involvement and the presence of greatly elongated dermal villi.
See also OMIM:124200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00860823G → E in DD. 1 PublicationCorresponds to variant rs28929478dbSNPEnsembl.1
Natural variantiVAR_00860939N → T in DD. 1 Publication1
Natural variantiVAR_06339841Missing in DD; comedonal type. 1 Publication1
Natural variantiVAR_00861047K → KMFLTGK in DD. 1
Natural variantiVAR_00861165L → S in DD; severe form. 1
Natural variantiVAR_008612131R → Q in DD. Corresponds to variant rs121912738dbSNPEnsembl.1
Natural variantiVAR_008613160P → L in DD. 1
Natural variantiVAR_008614186S → P in DD. 1
Natural variantiVAR_008615211G → D in DD; severe form. 1
Natural variantiVAR_008616223V → M in DD. 1
Natural variantiVAR_008617268C → F in DD; haemorrhagic lesions. Corresponds to variant rs121912733dbSNPEnsembl.1
Natural variantiVAR_008618310G → V in DD. 1
Natural variantiVAR_008619318C → R in DD; severe form. 1
Natural variantiVAR_008620348I → T in DD. 1
Natural variantiVAR_009508357T → K in DD. 1 Publication1
Natural variantiVAR_008621412E → G in DD. 1
Natural variantiVAR_008622495S → F in DD. 1 Publication1
Natural variantiVAR_008623560C → R in DD; neuropsychiatric phenotype. 1 PublicationCorresponds to variant rs121912734dbSNPEnsembl.1
Natural variantiVAR_008624675F → S in DD; multiple neuropsychiatric features. 1
Natural variantiVAR_008625683K → E in DD; depression. 1
Natural variantiVAR_008626702D → N in DD; moderate form. 1
Natural variantiVAR_008627745A → D in DD; moderate form. 1
Natural variantiVAR_009509749G → R in DD. 1 Publication1
Natural variantiVAR_008628754Missing in DD. 1
Natural variantiVAR_008629765S → L in DD. 1 Publication1
Natural variantiVAR_008630767N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype. Corresponds to variant rs121912732dbSNPEnsembl.1
Natural variantiVAR_008631769G → R in DD. Corresponds to variant rs121912736dbSNPEnsembl.1
Natural variantiVAR_008632803A → T in DD; mild/moderate form. 1
Natural variantiVAR_008633838A → P in DD; severe form; petit mal epilepsy. 1
Natural variantiVAR_008634843V → F in DD; depression. 1
Natural variantiVAR_008635875C → G in DD; retinitis pigmentosa. 1
Natural variantiVAR_008636920S → Y in DD; mild/moderate/severe form; one patient with epilepsy. 1
Natural variantiVAR_008637943H → R in DD; learning difficulties. 1
Natural variantiVAR_008638975P → R in DD. 1

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

DisGeNETi488.
MalaCardsiATP2A2.
MIMi101900. phenotype.
124200. phenotype.
OpenTargetsiENSG00000174437.
Orphaneti79151. Acrokeratosis verruciformis of Hopf.
218. Darier disease.
PharmGKBiPA71.

Chemistry databases

ChEMBLiCHEMBL3901.

Polymorphism and mutation databases

BioMutaiATP2A2.
DMDMi114312.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000461961 – 1042Sarcoplasmic/endoplasmic reticulum calcium ATPase 2Add BLAST1042

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei38PhosphoserineBy similarity1
Modified residuei294Nitrated tyrosine1 Publication1
Modified residuei295Nitrated tyrosine1 Publication1
Modified residuei441PhosphothreonineBy similarity1
Modified residuei531PhosphoserineBy similarity1
Modified residuei580PhosphoserineCombined sources1
Modified residuei663PhosphoserineCombined sources1

Post-translational modificationi

Nitrated under oxidative stress. Nitration on the two tyrosine residues inhibits catalytic activity.1 Publication

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

EPDiP16615.
MaxQBiP16615.
PaxDbiP16615.
PeptideAtlasiP16615.
PRIDEiP16615.

PTM databases

iPTMnetiP16615.
PhosphoSitePlusiP16615.
SwissPalmiP16615.

Expressioni

Tissue specificityi

Isoform 1 is widely expressed in smooth muscle and nonmuscle tissues such as in adult skin epidermis, with highest expression in liver, pancreas and lung, and intermediate expression in brain, kidney and placenta. Also expressed at lower levels in heart and skeletal muscle. Isoforms 2 and 3 are highly expressed in the heart and slow twitch skeletal muscle. Expression of isoform 3 is predominantly restricted to cardiomyocytes and in close proximity to the sarcolemma. Both isoforms are mildly expressed in lung, kidney, liver, pancreas and placenta. Expression of isoform 3 is amplified during monocytic differentiation and also observed in the fetal heart.3 Publications

Gene expression databases

BgeeiENSG00000174437.
CleanExiHS_ATP2A2.
ExpressionAtlasiP16615. baseline and differential.
GenevisibleiP16615. HS.

Organism-specific databases

HPAiHPA062605.
HPA067892.

Interactioni

Subunit structurei

Interacts with sarcolipin (SLN) (By similarity). Interacts with phospholamban (PLN) (By similarity). Interacts with myoregulin (MRLN) (By similarity). Interacts with DWORF (By similarity). Isoform 1 interacts with TRAM2 (via C-terminus) (PubMed:14749390). Interacts with HAX1 (PubMed:18971376). Interacts with S100A8 and S100A9 (By similarity). Interacts with SLC35G1 and STIM1 (PubMed:22084111). Interacts with TMEM203 (PubMed:25996873). Interacts with TMEM64 and PDIA3 (By similarity).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
OPRD1P411433EBI-358933,EBI-2624456

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • protein C-terminus binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106978. 70 interactors.
DIPiDIP-33868N.
IntActiP16615. 65 interactors.
MINTiMINT-4991144.
STRINGi9606.ENSP00000440045.

Structurei

3D structure databases

ProteinModelPortaliP16615.
SMRiP16615.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni370 – 400Interaction with phospholamban 1By similarityAdd BLAST31
Regioni575 – 594Interaction with HAX11 PublicationAdd BLAST20
Regioni787 – 807Interaction with phospholamban 2By similarityAdd BLAST21
Regioni788 – 1042Interaction with TMEM64 and PDIA3By similarityAdd BLAST255

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0202. Eukaryota.
COG0474. LUCA.
GeneTreeiENSGT00850000132256.
HOGENOMiHOG000265621.
HOVERGENiHBG105648.
InParanoidiP16615.
KOiK05853.
OMAiDDMIFLG.
OrthoDBiEOG091G01LE.
PhylomeDBiP16615.
TreeFamiTF300651.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
IPR030327. SERCA2.
[Graphical view]
PANTHERiPTHR24093:SF234. PTHR24093:SF234. 2 hits.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF08282. Hydrolase_3. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Note: SERCA2 transcripts differ only in their 3'-UTR region and are expressed in a tissue-specific manner.
Isoform 1 (identifier: P16615-1) [UniParc]FASTAAdd to basket
Also known as: ATP2A2B, Class 2-4, HK1, SERCA2b

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL
60 70 80 90 100
ELVIEQFEDL LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA
110 120 130 140 150
NAIVGVWQER NAENAIEALK EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI
160 170 180 190 200
VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL TGESVSVIKH TDPVPDPRAV
210 220 230 240 250
NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV ATEQERTPLQ
260 270 280 290 300
QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
310 320 330 340 350
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS
360 370 380 390 400
DKTGTLTTNQ MSVCRMFILD RVEGDTCSLN EFTITGSTYA PIGEVHKDDK
410 420 430 440 450
PVNCHQYDGL VELATICALC NDSALDYNEA KGVYEKVGEA TETALTCLVE
460 470 480 490 500
KMNVFDTELK GLSKIERANA CNSVIKQLMK KEFTLEFSRD RKSMSVYCTP
510 520 530 540 550
NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTSGV KQKIMSVIRE
560 570 580 590 600
WGSGSDTLRC LALATHDNPL RREEMHLEDS ANFIKYETNL TFVGCVGMLD
610 620 630 640 650
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK
660 670 680 690 700
AFTGREFDEL NPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT
710 720 730 740 750
GDGVNDAPAL KKAEIGIAMG SGTAVAKTAS EMVLADDNFS TIVAAVEEGR
760 770 780 790 800
AIYNNMKQFI RYLISSNVGE VVCIFLTAAL GFPEALIPVQ LLWVNLVTDG
810 820 830 840 850
LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG CYVGAATVGA
860 870 880 890 900
AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFEGVDCAIF ESPYPMTMAL
910 920 930 940 950
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE
960 970 980 990 1000
PLPLIFQITP LNVTQWLMVL KISLPVILMD ETLKFVARNY LEPGKECVQP
1010 1020 1030 1040
ATKSCSFSAC TDGISWPFVL LIMPLVIWVY STDTNFSDMF WS
Note: Ubiquitous housekeeping isoform.
Length:1,042
Mass (Da):114,757
Last modified:August 1, 1990 - v1
Checksum:i5462FF2DA7FB630A
GO
Isoform 2 (identifier: P16615-2) [UniParc]FASTAAdd to basket
Also known as: ATP2A2A, Class 1, HK2, SERCA2a

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → AILE

Note: Cardiac/slow twitch, muscle specific isoform. Has a lower affinity for calcium and a higher catalytic turnover rate.
Show »
Length:997
Mass (Da):109,691
Checksum:iDD57D12A2B24FEC1
GO
Isoform 3 (identifier: P16615-3) [UniParc]FASTAAdd to basket
Also known as: SERCA2C

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → VLSSEL

Note: May be due to intron retention. Shows a lower apparent affinity for cytosolic calcium than isoform 2 and a catalytic turnover rate similar to isoform 1.
Show »
Length:999
Mass (Da):109,893
Checksum:iF6BE03E546453B24
GO
Isoform 4 (identifier: P16615-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     155-181: Missing.

Note: No experimental confirmation available.
Show »
Length:1,015
Mass (Da):111,847
Checksum:i6C99B5C382834A63
GO
Isoform 5 (identifier: P16615-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     994-1042: GKECVQPATKSCSFSACTDGISWPFVLLIMPLVIWVYSTDTNFSDMFWS → DIIK

Note: No experimental confirmation available.
Show »
Length:997
Mass (Da):109,734
Checksum:iD570A12D5B24FEC1
GO

Sequence cautioni

The sequence BAG57266 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00860823G → E in DD. 1 PublicationCorresponds to variant rs28929478dbSNPEnsembl.1
Natural variantiVAR_00860939N → T in DD. 1 Publication1
Natural variantiVAR_06339841Missing in DD; comedonal type. 1 Publication1
Natural variantiVAR_00861047K → KMFLTGK in DD. 1
Natural variantiVAR_00861165L → S in DD; severe form. 1
Natural variantiVAR_008612131R → Q in DD. Corresponds to variant rs121912738dbSNPEnsembl.1
Natural variantiVAR_008613160P → L in DD. 1
Natural variantiVAR_008614186S → P in DD. 1
Natural variantiVAR_008615211G → D in DD; severe form. 1
Natural variantiVAR_008616223V → M in DD. 1
Natural variantiVAR_008617268C → F in DD; haemorrhagic lesions. Corresponds to variant rs121912733dbSNPEnsembl.1
Natural variantiVAR_008618310G → V in DD. 1
Natural variantiVAR_008619318C → R in DD; severe form. 1
Natural variantiVAR_008620348I → T in DD. 1
Natural variantiVAR_009508357T → K in DD. 1 Publication1
Natural variantiVAR_008621412E → G in DD. 1
Natural variantiVAR_008622495S → F in DD. 1 Publication1
Natural variantiVAR_008623560C → R in DD; neuropsychiatric phenotype. 1 PublicationCorresponds to variant rs121912734dbSNPEnsembl.1
Natural variantiVAR_017532602P → L in AKV; loss of activity. 1 PublicationCorresponds to variant rs121912737dbSNPEnsembl.1
Natural variantiVAR_008624675F → S in DD; multiple neuropsychiatric features. 1
Natural variantiVAR_008625683K → E in DD; depression. 1
Natural variantiVAR_008626702D → N in DD; moderate form. 1
Natural variantiVAR_008627745A → D in DD; moderate form. 1
Natural variantiVAR_009509749G → R in DD. 1 Publication1
Natural variantiVAR_008628754Missing in DD. 1
Natural variantiVAR_008629765S → L in DD. 1 Publication1
Natural variantiVAR_008630767N → S in DD; haemorrhagic lesions and neuropsychiatric phenotype. Corresponds to variant rs121912732dbSNPEnsembl.1
Natural variantiVAR_008631769G → R in DD. Corresponds to variant rs121912736dbSNPEnsembl.1
Natural variantiVAR_008632803A → T in DD; mild/moderate form. 1
Natural variantiVAR_008633838A → P in DD; severe form; petit mal epilepsy. 1
Natural variantiVAR_008634843V → F in DD; depression. 1
Natural variantiVAR_008635875C → G in DD; retinitis pigmentosa. 1
Natural variantiVAR_008636920S → Y in DD; mild/moderate/severe form; one patient with epilepsy. 1
Natural variantiVAR_008637943H → R in DD; learning difficulties. 1
Natural variantiVAR_008638975P → R in DD. 1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_039392155 – 181Missing in isoform 4. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_000358994 – 1042GKECV…DMFWS → AILE in isoform 2. 1 PublicationAdd BLAST49
Alternative sequenceiVSP_039393994 – 1042GKECV…DMFWS → VLSSEL in isoform 3. 1 PublicationAdd BLAST49
Alternative sequenceiVSP_039394994 – 1042GKECV…DMFWS → DIIK in isoform 5. CuratedAdd BLAST49

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23114 mRNA. Translation: AAA53193.1.
M23116 Genomic DNA. Translation: AAA52757.1.
M23115 mRNA. Translation: AAA53194.1.
M23278, M23116 Genomic DNA. Translation: AAA52758.1.
AC006088 Genomic DNA. No translation available.
BC035588 mRNA. Translation: AAH35588.1.
AK293877 mRNA. Translation: BAG57266.1. Different initiation.
AY186578 mRNA. Translation: AAO47398.1.
CCDSiCCDS9143.1. [P16615-2]
CCDS9144.1. [P16615-1]
PIRiA31981.
B31981.
RefSeqiNP_001672.1. NM_001681.3. [P16615-2]
NP_733765.1. NM_170665.3. [P16615-1]
XP_005253945.1. XM_005253888.2. [P16615-3]
XP_011536704.1. XM_011538402.2. [P16615-3]
UniGeneiHs.506759.

Genome annotation databases

EnsembliENST00000308664; ENSP00000311186; ENSG00000174437. [P16615-2]
ENST00000539276; ENSP00000440045; ENSG00000174437. [P16615-1]
GeneIDi488.
KEGGihsa:488.
UCSCiuc001tqk.5. human. [P16615-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M23114 mRNA. Translation: AAA53193.1.
M23116 Genomic DNA. Translation: AAA52757.1.
M23115 mRNA. Translation: AAA53194.1.
M23278, M23116 Genomic DNA. Translation: AAA52758.1.
AC006088 Genomic DNA. No translation available.
BC035588 mRNA. Translation: AAH35588.1.
AK293877 mRNA. Translation: BAG57266.1. Different initiation.
AY186578 mRNA. Translation: AAO47398.1.
CCDSiCCDS9143.1. [P16615-2]
CCDS9144.1. [P16615-1]
PIRiA31981.
B31981.
RefSeqiNP_001672.1. NM_001681.3. [P16615-2]
NP_733765.1. NM_170665.3. [P16615-1]
XP_005253945.1. XM_005253888.2. [P16615-3]
XP_011536704.1. XM_011538402.2. [P16615-3]
UniGeneiHs.506759.

3D structure databases

ProteinModelPortaliP16615.
SMRiP16615.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106978. 70 interactors.
DIPiDIP-33868N.
IntActiP16615. 65 interactors.
MINTiMINT-4991144.
STRINGi9606.ENSP00000440045.

Chemistry databases

ChEMBLiCHEMBL3901.

Protein family/group databases

TCDBi3.A.3.2.7. the p-type atpase (p-atpase) superfamily.

PTM databases

iPTMnetiP16615.
PhosphoSitePlusiP16615.
SwissPalmiP16615.

Polymorphism and mutation databases

BioMutaiATP2A2.
DMDMi114312.

Proteomic databases

EPDiP16615.
MaxQBiP16615.
PaxDbiP16615.
PeptideAtlasiP16615.
PRIDEiP16615.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000308664; ENSP00000311186; ENSG00000174437. [P16615-2]
ENST00000539276; ENSP00000440045; ENSG00000174437. [P16615-1]
GeneIDi488.
KEGGihsa:488.
UCSCiuc001tqk.5. human. [P16615-1]

Organism-specific databases

CTDi488.
DisGeNETi488.
GeneCardsiATP2A2.
HGNCiHGNC:812. ATP2A2.
HPAiHPA062605.
HPA067892.
MalaCardsiATP2A2.
MIMi101900. phenotype.
108740. gene.
124200. phenotype.
neXtProtiNX_P16615.
OpenTargetsiENSG00000174437.
Orphaneti79151. Acrokeratosis verruciformis of Hopf.
218. Darier disease.
PharmGKBiPA71.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0202. Eukaryota.
COG0474. LUCA.
GeneTreeiENSGT00850000132256.
HOGENOMiHOG000265621.
HOVERGENiHBG105648.
InParanoidiP16615.
KOiK05853.
OMAiDDMIFLG.
OrthoDBiEOG091G01LE.
PhylomeDBiP16615.
TreeFamiTF300651.

Enzyme and pathway databases

BioCyciZFISH:HS10797-MONOMER.
ReactomeiR-HSA-1912420. Pre-NOTCH Processing in Golgi.
R-HSA-418359. Reduction of cytosolic Ca++ levels.
R-HSA-5578775. Ion homeostasis.
R-HSA-936837. Ion transport by P-type ATPases.
SignaLinkiP16615.
SIGNORiP16615.

Miscellaneous databases

ChiTaRSiATP2A2. human.
GenomeRNAii488.
PROiP16615.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000174437.
CleanExiHS_ATP2A2.
ExpressionAtlasiP16615. baseline and differential.
GenevisibleiP16615. HS.

Family and domain databases

Gene3Di1.20.1110.10. 2 hits.
2.70.150.10. 2 hits.
3.40.1110.10. 1 hit.
InterProiIPR006068. ATPase_P-typ_cation-transptr_C.
IPR004014. ATPase_P-typ_cation-transptr_N.
IPR023299. ATPase_P-typ_cyto_domN.
IPR018303. ATPase_P-typ_P_site.
IPR023298. ATPase_P-typ_TM_dom.
IPR008250. ATPase_P-typ_transduc_dom_A.
IPR023214. HAD-like_dom.
IPR005782. P-type_ATPase_IIA.
IPR001757. P_typ_ATPase.
IPR030327. SERCA2.
[Graphical view]
PANTHERiPTHR24093:SF234. PTHR24093:SF234. 2 hits.
PfamiPF00689. Cation_ATPase_C. 1 hit.
PF00690. Cation_ATPase_N. 1 hit.
PF00122. E1-E2_ATPase. 1 hit.
PF08282. Hydrolase_3. 1 hit.
[Graphical view]
PRINTSiPR00120. HATPASE.
SMARTiSM00831. Cation_ATPase_N. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
SSF81660. SSF81660. 1 hit.
TIGRFAMsiTIGR01116. ATPase-IIA1_Ca. 1 hit.
TIGR01494. ATPase_P-type. 2 hits.
PROSITEiPS00154. ATPASE_E1_E2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAT2A2_HUMAN
AccessioniPrimary (citable) accession number: P16615
Secondary accession number(s): A6NDN7
, B4DF05, P16614, Q86VJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: November 30, 2016
This is version 201 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.